Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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The complex proton spin-echo decay curve was recorded for human serum albumin (SA) solutions with different concentrations in normal and heavy water. The curve included three fast-decaying components for SA, in addition to the slow-decaying component for the water. The total amplitude of these three components roughly corresponded to the number of protons in the SA (with isotopic exchange taken into account); the component ratio remained constant at different concentrations and different temperatures between 4 and 39 degrees. The relatively slow-decaying protein component, which accounted for similar to 10% of the SA protons, was produced by the side chains of the protein. The presence of two other faster-decaying SA components with approximately equal amplitudes indicated that only about half of the remaining protons in the SA macromolecule are incorporated into the comparatively rigid globule, the other half belonging to groups with high conformational lability in aqueous solution. The activation energy for the aqueous component was close to that for pure water, while the activation energies for the protein components were roughly twice as large.
Mol Biol 1975 Jan
PMID:Investigation of the conformational lability of serum albumin macromolecules in aqueous solution by the NMR spin-echo method. 23 8

The interactions of the parasympatholytic drugs adiphenin, adiphenin H and propanthelin and the structurally related compounds, diphenhydramine, D-propoxyphene and methadone with bovine serum albumin (BSA) are studied by equilibrium dialysis and ultracentrifugation. The results show that BSA has a few binding sites (n less than 10) for the mentioned drugs. The association between the compounds under study and BSA are relatively weak. The binding constants are in the range of 10(3) l/Mol.
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PMID:[Interactions of some parasympatholytics and structurally similar drugs with bovine serum albumin]. 24 Mar 66

Compounds were studied that inhibit the oxidative degradation of human serum albumin by peroxidase and the enzyme model, iron hydroxide. Differences between the two oxidants gave clues for the mechanism of inhibition. The inhibitors studied were inorganic anions, phosphate, sulfate, carbonate and molybdate; organic anions, decanoate and glycocholate; and the nonionic species, glycogen. Such inhibitors might be considered as adjuvants in senescence: by decreasing the rate of enzymic oxidation of essential body proteins, they would, in the course of aging, reduce some of the physiological changes occurring as a result of accumulation of degraded protein.
Mol Biol Rep 1979 Feb 15
PMID:Inhibitors of oxidative degradation of protein: gerontological implications. 44 Feb 99

The mobility of separate sites of the water-protein matrix depending on temperature and degree of hydration has been investigated by means of spin labels covalently attached to surface layers of proteins (alpha-chymotrypsin and human serum albumin) and also by a spin probe in a hydrophobic "pocket" of human serum albumin. The results obtained are compared with the data on the mobility of gamma-resonance labels (57Fe) firmly bound with the protein matrix in the same samples. At certain temperature and degree of hydration both spin and gamma-resonance label show an increase in mobility. With the degree of hydration increasing one may observe a simultaneous increase in energy and in entropy of activation: rotatory diffusion of spin labels, i. e., a compensation effect takes place which confirms the concept expressed earlier that cooperation of water-protein interactions is the main reason of CEF. It should be noted that at P/PS greater than 0.8 the values of delta E =7 divided by 10 kcal/mole, and delta S not equal to = 9 divided by 11 e. e. are specific to glycerol-like systems, i. e., under these conditions (P/Ps greater than 0.8) the water-protein layer has glycerol-like properties.
Mol Biol (Mosk)
PMID:[Effect of temperature and degree of hydration on the mobility of spin labels in surface layers of proteins]. 46 Feb 2

The aim of this work was to investigate the interrelationship between RNA biosynthesis and that of protein in chick liver during experimental coccidiosis induced by E. tenella. The peculiarity of this model is that in the course of this disease protein synthesis is significantly intensified inspite of the fact that the rate of the biosynthesis is rather high under normal conditions. It has been shown that 4 to 6 days after infection incorporation of labeled amino acids into proteins from chick liver subcellular fractions is greatly increased. The most pronounced changes are in ribosomal and mitochondrial fractions as well as in the postribosomal supernatant. At the same time the specific radioactivity of serum albumin excreted by liver was increased by factor 3. These changes in protein biosynthesis are associated with a significant increase of both the content and intensity of biosynthesis of high molecular weight precursors of rRNA as well as with those of mature 18S rRNA. The amount of 28S rRNA and mRNA per cell is practically without any changes whereas the mRNA turnover is somewhat more extensive. The selective accumulation of 18S rRNA is suggested to be responsible for the intensification of protein biosynthesis.
Mol Biol (Mosk)
PMID:[RNA biosynthesis and regulation of protein biosynthesis in the liver of chicks with experimental coccidiosis]. 56 78

1. 1alpha,25-Dihydroxy-25-hemisuccinate cholecalciferol has been synthesized and conjugated to bovine serum albumin. 2. This conjugate is immunogenic; when injected into rabbits antibodies of high affinity for 1alpha,25-dihydroxycholecalciferol were obtained. 3. Vitamin D metabolites lacking the 1alpha-hydroxy group were of lower cross-reactivity with the antibodies. 4. By using these antibodies and 1alpha,25-[23,24-3H]dihydroxycholecalciferol as tracer a sensitive radioimmunoassay has been developed capable of detecting 20 pg of 1alpha,25-dihydroxycholecalciferol.
Clin Sci Mol Med 1978 Mar
PMID:A radioimmunoassay for 1,25-dihydroxycholecalciferol. 63 Aug 9

4-N (p-sulfoaniline),5-methoxy,1,2-benzoquinon (1) is bound by hydrophobic regions of the native molecule of bovine serum albumin (BSA). In the temperature interval 0--65 degrees C the interaction characteristics such as energy, entropy and the average number of the binding sites on a BSA molecule were determined. Under experimental conditions BSA is found in at least in two equilibrium conformational states distinguished by quantity of hydrophobic regions capable of binding with 1. Below 17 degrees C no conformational changes of BSA was observed. With the increase of temperature from 17 to 47 degrees C the equilibrium is driven in the direction of protein form with the hydrophobic binding sites which are more available for the solvent. Heating above 47 degrees C produces "predenaturation" structural changes in the BSA molecule. Hydrophobic regions of the BSA have different thermal stability.
Mol Biol (Mosk)
PMID:[Study of temperature-dependent conformational changes in serum albumin using an adsorbed dye]. 63 87

The thermal transitions of native lysozyme and a well-characterized cross-linked derivative of lysozyme [Imoto, T., and Rupley, J. A. (1973), J. Mol. Biol. 80, 657] have been studied in 1.94 M guanidine hydrochloride at pH 2. The observed increase in the melting temperature from 32.4 degrees C for native lysozyme to 61.8 degrees C for the cross-linked derivative corresponds to a calculated 5.2 kcal/mol increase in the free energy of denaturation. This free-energy change is attributed to the decreased entropy of the unfolded polypeptide chain following introduction of a cross-link and is shown to compare well with theoretical predictions. The possibility that an introduction of a cross-link could also affect the enthalpy of an unfolded protein was investigated. The heats of reduction of bovine serum albumin and lysozyme by dithioerythritol in 6 M guanidine hydrochloride were determined and compared to that for the model peptide, oxidized glutathione. The near identity of the observed heats was taken as evidence that the introduction of cross-links into a random-coil protein does not, in general, introduce strain.
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PMID:Thermodynamics of protein cross-links. 64 96

1. Filters comprising multiple layers of rabbit renal tubular basement membrane were constructed with conventional pressure filtration chambers. The effects of concentration-polarization on the behaviour of these filters was assessed by studying the filtration of proteins and of serum under turbulent (stirred) and unstirred conditions. 2. With stirring bovine serum albumin was effectively rejected by the filter barriers (sigma = 0.95) but rejection was diminished (sigma = 0.18) without stirring. The hydraulic permeability of the filters also fell without stirring. 3. In the presence of horse immunoglobulin G, a wholly rejected protein, the rejection of cytochrome c was increased and hydraulic flux was reduced. 4. Filtration studies of serum showed that serum protein was effectively rejected with stirring (sigma greater than 0.999) but rejection diminished when stirring ceased (sigma = 0.98). Albumin was the only protein detected in the filtrate with stirring but alpha- and beta- globulins appeared when stirring ceased. 5. These results show that concentration-polarization markedly affects the behaviour of these basement membrane filters in vitro, since without stirring a polarization layer of rejected protein is formed, which reduces hydraulic permeability and results in increased protein permeation through the filter.
Clin Sci Mol Med 1978 Jul
PMID:Effects of concentration-polarization on the filtration of proteins through filters constructed from isolated renal basement membrane. 66 63

The binding to neutrophil leukoyctes of human serum albumin (HSA), which is chemokinetic for leukocytes, i.e. influences their rate of locomotion, and of alkali-denatured HSA, which is chemotactic for leukocytes, i.e. influences their direction of locomotion, was studied. Native serum albumin showed low affinity binding to the neutrophil surface. Denatured serum albumin showed saturable binding with a Ka of approximately 1-(6) litres per mole to about 10(6) binding sites per cell. Another protein chemotactic factor, alpha5-casein, gave similar binding. These results exclude that chemotactic reactions to denatured proteins are mediated in a completely non-specific manner and suggest the presence on the cell of a restricted number of defined recognition sites. Binding was reduced following treatment of the cells with either of two lipid-specific bacterial toxins, perfringolysin, the theta-toxin of Clostridium perfringens, an oxygen-labile cholesterol-specific toxin, and Staphylococcus aureus Sphingomyelinase C. Both have previously been shown to reduce chemotactic reactions and both were used at doses which did not reduce cell viability. These results suggest an important, and possiblly direct, role for membrane lipid in the binding sites for chemotactic factors. Visual analysis of the behaviour of perfringolysin-treated neutrophils showed that these cells were still capable of chemotactic locomotion. The cells appeared to be less efficient than normal in detecting chemotactic gradients only when at a distance from the gradient source, a finding which is consistent with reduced binding of the chemotactic factor to the cell surface.
Mol Cell Biochem 1978 Jun 15
PMID:Binding of protein chemotactic factors to the surfaces of neutrophil leukocytes and its modification with lipid-specific bacterial toxins. 67 3


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